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Published Online October 4, 2007
Science DOI: 10.1126/science.1145980

Reports

Submitted on June 4, 2007
Accepted on September 21, 2007

Nanomechanical Basis of Selective Gating by the Nuclear Pore Complex

Roderick Y.H. Lim 1*, Birthe Fahrenkrog 1*, Joachim Köser 2, Kyrill Schwarz-Herion 1, Jie Deng 3, Ueli Aebi 1

1 M.E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, Basel 4056, Switzerland.
2 M.E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, Basel 4056, Switzerland. ; Present address: Concentris GmbH, Davidsbodenstrasse 63, P.O. Box 340, Basel 4012, Switzerland.
3 Institute of Materials Research and Engineering (IMRE), 3 Research Link, Singapore 117602, Singapore.

* To whom correspondence should be addressed.
Roderick Y.H. Lim , E-mail: roderick.lim{at}unibas.ch
Birthe Fahrenkrog , E-mail: birthe.fahrenkrog{at}unibas.ch

The nuclear pore complex regulates cargo transport between the cytoplasm and the nucleus. We set out to correlate the governing biochemical interactions to the nanoscopic responses of the phenylalanine-glycine (FG)-rich nucleoporin domains, which are involved in attenuating or promoting cargo translocation. We found that binding interactions with the transport receptor, karyopherin-{beta}1, caused the FG-domains of Nup153 to collapse into compact molecular conformations. This effect was reversed by the action of RanGTP, which returned the FG-domains into a polymer brush-like, entropic barrier conformation. Similar effects were observed in Xenopus oocyte nuclei in situ. Thus, we anticipate that the reversible collapse of the FG-domains may play a significant role in regulating nucleocytoplasmic transport.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)